id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-102842-51n5mnjb	Węglarz-Tomczak, Ewelina	Ebselen as a highly active inhibitor of PLProCoV2	2020-05-17		.txt	text/plain	3320	196	56	In conclusion, we show that ebselen inhibits the activity of the essential viral enzyme papain-like protease (PLpro) from SARS-COV-2 in low micromolar range. Here, we demonstrate that ebselen inhibits activity of the essential viral enzyme, namely, papain-like protease (PL pro ) from SARS-CoV-2 (PL pro CoV2) in low micromolar range. We applied ebselen as a possible inhibitor and, indeed, it suppresses PL Pro activity from CoV2 with inhibition constants approximately equal 2 μM (Table 1 and Figure 3 ). Our results were further illustrated by the use of molecular modeling to study the binding mode of ebselen with PL Pro SARS ( Figure 4 ) and PL Pro CoV2 (Figure 4 and 5) . This study confirmed our primary assumption that ebselen binds to the PL Pro CoV2 active site covalently and, thus, convinced us of our hypothesis about an irreversible mechanism of inhibition.	./cache/cord-102842-51n5mnjb.txt	./txt/cord-102842-51n5mnjb.txt